1.3.5 Increasing concentrations of H+(with a decrease of ph)or CO2 lowers the O2 affinity of hemoglobin(H+ and co, has no effect on o2 affinity of myoglobin). This is called Bohr effect, which helps the release of o, in the capillaries of actively metabolizing tissues (melecular mechanism?) 1.3.6 One molecule of 2, 3-diphosphoglycerate (BPG binds to the central cavity of one tetramer of hemoglobin, which lowers its O2 affinity. 1.3.7 Fetal hemoglobin (HbF)binds BPg less strongly than does hemoglobin a (adult) and consequently has a higher oxygen affinity(physiological function? Extraction of o2 from the mother)1.3.5 Increasing concentrations of H+ (with a decrease of pH) or CO2 lowers the O2 affinity of hemoglobin (H+ and CO2 has no effect on O2 affinity of myoglobin). This is called Bohr effect, which helps the release of O2 in the capillaries of actively metabolizing tissues. (melecular mechanism?) 1.3.6 One molecule of 2,3-diphosphoglycerate (BPG) binds to the central cavity of one tetramer of hemoglobin, which lowers its O2 affinity. 1.3.7 Fetal hemoglobin (HbF) binds BPG less strongly than does hemoglobin A (adult) and consequently has a higher oxygen affinity. (physiological function? Extraction of O2 from the mother)